Isoelectric focusing analysis showed a single angiotensin II (All)-receptor complex migrating to pI 6·8 in nuclear preparations, while in plasma membranes a charge heterogeneity of the All receptor subtype AT1 was observed. 125I-Labelled All binding sites were found in intact nuclei and were not detected in nuclear extracts. Neither disruption of cytoskeletal elements by colchicine nor prevention of endosome acidification by chloroquine had any effect on nuclear accumulation of AIL Nevertheless, the monovalent ionophore monensin inhibited nuclear accumulation of 125I-Labelled All. Our findings are consistent with the hypothesis that processing through the Golgi apparatus could be involved in the nuclear accumulation of AIL
Journal of Endocrinology (1994) 143, 449–453
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